ID   BZRD_BACCE              Reviewed;         249 AA.
AC   Q8RJB2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Benzil reductase ((S)-benzoin forming);
DE            EC=1.1.1.320;
GN   Name=yueD;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Tim-r01;
RX   PubMed=11745140; DOI=10.1002/bit.1191;
RA   Maruyama R., Nishizawa M., Itoi Y., Ito S., Inoue M.;
RT   "Isolation and expression of a Bacillus cereus gene encoding benzil
RT   reductase.";
RL   Biotechnol. Bioeng. 75:630-633(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=NBRC 3563;
RX   PubMed=11796169; DOI=10.1016/s0168-1656(01)00426-6;
RA   Maruyama R., Nishizawa M., Itoi Y., Ito S., Inoue M.;
RT   "The enzymes with benzil reductase activity conserved from bacteria to
RT   mammals.";
RL   J. Biotechnol. 94:157-169(2002).
CC   -!- FUNCTION: Reduces benzil stereospecifically to (S)-benzoin. Can also
CC       reduce 1-phenyl-1,2-propanedione, 1,4-naphthoquinone, 1-(4-methyl-
CC       phenyl)-2-phenyl-ethane-1,2-dione, 1-(4-fluoro-phenyl)-2-phenyl-ethane-
CC       1,2-dione, methyl benzoylformate, p-nitrobenzaldehyde in decreasing
CC       order. {ECO:0000269|PubMed:11745140}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-benzoin + NADP(+) = benzil + H(+) + NADPH;
CC         Xref=Rhea:RHEA:25968, ChEBI:CHEBI:15378, ChEBI:CHEBI:51507,
CC         ChEBI:CHEBI:51510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.320; Evidence={ECO:0000269|PubMed:11745140};
CC   -!- ACTIVITY REGULATION: Inhibited by Cibacron blue 3 GA.
CC       {ECO:0000269|PubMed:11796169}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27.6 uM for 1,4-naphthoquinone (with NADPH at 37 degrees Celsius
CC         and pH 6.5) {ECO:0000269|PubMed:11796169};
CC         KM=42 uM for 1-phenyl-1,2-propanedione (with NADPH at 37 degrees
CC         Celsius and pH 6.5) {ECO:0000269|PubMed:11796169};
CC         KM=261 uM for p-nitrobenzaldehyde (with NADPH and at 37 degrees
CC         Celsius and pH 6.5) {ECO:0000269|PubMed:11796169};
CC         KM=584 uM for 1-(4-fluoro-phenyl)-2-phenyl-ethane-1,2-dione (with
CC         NADPH at 37 degrees Celsius and pH 6.5)
CC         {ECO:0000269|PubMed:11796169};
CC         KM=611 uM for 1-(4-methyl-phenyl)-2-phenyl-ethane-1,2-dione (with
CC         NADPH at 37 degrees Celsius and pH 6.5)
CC         {ECO:0000269|PubMed:11796169};
CC         KM=768 uM for benzil (with NADPH at 37 degrees Celsius and pH 6.5)
CC         {ECO:0000269|PubMed:11796169};
CC         KM=1400 uM for methyl benzoylformate (with NADPH and at 37 degrees
CC         Celsius and pH 6.5) {ECO:0000269|PubMed:11796169};
CC       pH dependence:
CC         Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:11796169};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius (at pH 6.5).
CC         {ECO:0000269|PubMed:11796169};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11796169}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB049404; BAB86001.1; -; Genomic_DNA.
DR   EMBL; AB052931; BAB86009.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RJB2; -.
DR   SMR; Q8RJB2; -.
DR   STRING; 1396.DJ87_1410; -.
DR   KEGG; ag:BAB86001; -.
DR   eggNOG; COG1028; Bacteria.
DR   BioCyc; MetaCyc:MON-17022; -.
DR   BRENDA; 1.1.1.320; 648.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102306; F:benzil reductase [(S)-benzoin-forming] activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN           1..249
FT                   /note="Benzil reductase ((S)-benzoin forming)"
FT                   /id="PRO_0000366975"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         5..27
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   249 AA;  27960 MW;  59EA0531AAB02DBA CRC64;
     MRYVIITGTS QGLGEAIATQ LLEESTTVIS ISRRENKELT KLAEQYNSNC IFHSLDLQDV
     HNLETNFKEI ISSIKEDNVS SIHLINNAGT VAPMKPIEKA ESEQFITNVH INLLAPMILT
     STFMKHTKEW KVDKRVINIS SGAGKNPYFG WGAYCTTKAG VNMFTQCVAT EEVEKEYPVK
     IVAFAPGVVD TNMQAQIRET AKEDFTNLDR FIALKEEGKL LSPEYVAKAI RNLLETEEFP
     QGEVIRIDE